1qi4

X-ray diffraction
2Å resolution

MUTANT (E219G) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH MALTOTETRAOSE

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glucan 1,4-alpha-maltotetraohydrolase Chain: A
Molecule details ›
Chain: A
Length: 429 amino acids
Theoretical weight: 47.34 KDa
Source organism: Pseudomonas stutzeri
Expression system: Escherichia coli
UniProt:
  • Canonical: P13507 (Residues: 22-450; Coverage: 81%)
Gene name: amyP
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 65.52Å b: 171.1Å c: 46.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 not available not available
Expression system: Escherichia coli